[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/oas1-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/oas1-wikipedia\/","headline":"OAS1 – Wikipedia","name":"OAS1 – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 2′-5′-oligoadenylate synthetase 1 is an enzyme that in humans is encoded by the","datePublished":"2019-05-02","dateModified":"2019-05-02","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","url":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","height":"1","width":"1"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/oas1-wikipedia\/","wordCount":5728,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x42′-5′-oligoadenylate synthetase 1 is an enzyme that in humans is encoded by the OAS1 gene.[5][6]This gene encodes a member of the 2-5A synthetase family, which include essential proteins involved in the innate immune response to viral infection.       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4The encoded protein is induced by interferons and uses adenosine triphosphate in 2′-specific nucleotidyl transfer reactions to synthesize 2′,5′-oligoadenylates (2-5As). These molecules activate latent RNase L, which results in both viral and endogenous RNA degradation and the inhibition of viral replication. The three known members of this gene family are located in a cluster on chromosome 12. Hypomorphic mutations in this gene have been associated with host susceptibility to viral infection, while gain-of-function variants can cause autoinflammatory immunodeficiency.[7] Alternatively spliced transcript variants encoding different isoforms have been described.[8]References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000089127 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000052776 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ Renault B, Hovnanian A, Bryce S, Chang JJ, Lau S, Sakuntabhai A, Monk S, Carter S, Ross CJ, Pang J, Twells R, Chamberlain S, Monaco AP, Strachan T, Kucherlapati R (Feb 1998). “A sequence-ready physical map of a region of 12q24.1”. Genomics. 45 (2): 271\u20138. doi:10.1006\/geno.1997.4888. PMID\u00a09344649.^ Nechiporuk T, Nechiporuk A, Sahba S, Figueroa K, Shibata H, Chen XN, Korenberg JR, de Jong P, Pulst SM (Nov 1997). “A high-resolution PAC and BAC map of the SCA2 region”. Genomics. 44 (3): 321\u20139. doi:10.1006\/geno.1997.4886. PMID\u00a09325053.^ Magg, T.; Okano, T.; Koenig, L. M.; Boehmer DFR; Schwartz, S. L.; Inoue, K.; Heimall, J.; Licciardi, F.; Ley-Zaporozhan, J.; Ferdman, R. M.; Caballero-Oteyza, A.; Park, E. N.; Calderon, B. M.; Dey, D.; Kanegane, H.; Cho, K.; Montin, D.; Reiter, K.; Griese, M.; Albert, M. H.; Rohlfs, M.; Gray, P.; Walz, C.; Conn, G. L.; Sullivan, K. E.; Klein, C.; Morio, T.; Hauck, F. (2021). “Heterozygous OAS1 gain-of-function variants cause an autoinflammatory immunodeficiency”. Sci Immunol. 6 (60): eabf9564. doi:10.1126\/sciimmunol.abf9564. PMC\u00a08392508. PMID\u00a034145065.^ “Entrez Gene: OAS1 2′,5′-oligoadenylate synthetase 1, 40\/46kDa”.Further reading[edit]Justesen J, Hartmann R, Kjeldgaard NO (2000). “Gene structure and function of the 2′-5′-oligoadenylate synthetase family”. Cell. Mol. Life Sci. 57 (11): 1593\u2013612. doi:10.1007\/PL00000644. PMID\u00a011092454. S2CID\u00a019154357.Ghosh SK, Kusari J, Bandyopadhyay SK,  et\u00a0al. (1991). “Cloning, sequencing, and expression of two murine 2′-5′-oligoadenylate synthetases. Structure-function relationships”. J. Biol. Chem. 266 (23): 15293\u20139. doi:10.1016\/S0021-9258(18)98615-1. PMID\u00a01651324.Silverman RH, Sengupta DN (1991). “Translational regulation by HIV leader RNA, TAT, and interferon-inducible enzymes”. J. Exp. Pathol. 5 (2): 69\u201377. PMID\u00a01708818.Saunders ME, Gewert DR, Tugwell ME,  et\u00a0al. (1985). “Human 2-5A synthetase: characterization of a novel cDNA and corresponding gene structure”. EMBO J. 4 (7): 1761\u20138. doi:10.1002\/j.1460-2075.1985.tb03848.x. PMC\u00a0554415. PMID\u00a02411547.Benech P, Mory Y, Revel M, Chebath J (1986). “Structure of two forms of the interferon-induced (2′-5′) oligo A synthetase of human cells based on cDNAs and gene sequences”. EMBO J. 4 (9): 2249\u201356. doi:10.1002\/j.1460-2075.1985.tb03922.x. PMC\u00a0554493. PMID\u00a02416561.Williams BR, Saunders ME, Willard HF (1986). “Interferon-regulated human 2-5A synthetase gene maps to chromosome 12”. Somat. Cell Mol. Genet. 12 (4): 403\u20138. doi:10.1007\/BF01570735. PMID\u00a02426799. S2CID\u00a013077134.Hovanessian AG, Laurent AG, Chebath J,  et\u00a0al. (1987). “Identification of 69-kd and 100-kd forms of 2-5A synthetase in interferon-treated human cells by specific monoclonal antibodies”. EMBO J. 6 (5): 1273\u201380. doi:10.1002\/j.1460-2075.1987.tb02364.x. PMC\u00a0553929. PMID\u00a02440675.Rutherford MN, Hannigan GE, Williams BR (1988). “Interferon-induced binding of nuclear factors to promoter elements of the 2-5A synthetase gene”. EMBO J. 7 (3): 751\u20139. doi:10.1002\/j.1460-2075.1988.tb02872.x. PMC\u00a0454386. PMID\u00a02456211.Benech P, Vigneron M, Peretz D,  et\u00a0al. (1988). “Interferon-responsive regulatory elements in the promoter of the human 2′,5′-oligo(A) synthetase gene”. Mol. Cell. Biol. 7 (12): 4498\u2013504. doi:10.1128\/MCB.7.12.4498. PMC\u00a0368134. PMID\u00a02830497.Wathelet MG, Clauss IM, Nols CB,  et\u00a0al. (1988). “New inducers revealed by the promoter sequence analysis of two interferon-activated human genes”. Eur. J. Biochem. 169 (2): 313\u201321. doi:10.1111\/j.1432-1033.1987.tb13614.x. PMID\u00a03121313.Wathelet MG, Szpirer J, Nols CB,  et\u00a0al. (1988). “Cloning and chromosomal location of human genes inducible by type I interferon”. Somat. Cell Mol. Genet. 14 (5): 415\u201326. doi:10.1007\/BF01534709. PMID\u00a03175763. S2CID\u00a042406993.Wathelet M, Moutschen S, Cravador A,  et\u00a0al. (1986). “Full-length sequence and expression of the 42 kDa 2-5A synthetase induced by human interferon”. FEBS Lett. 196 (1): 113\u201320. doi:10.1016\/0014-5793(86)80224-1. PMID\u00a03753689. S2CID\u00a038673605.Shiojiri S, Fukunaga R, Ichii Y, Sokawa Y (1986). “Structure and expression of a cloned cDNA for human (2′-5′)oligoadenylate synthetase”. J. Biochem. 99 (5): 1455\u201364. doi:10.1093\/oxfordjournals.jbchem.a135615. PMID\u00a03754863.Merlin G, Chebath J, Benech P,  et\u00a0al. (1983). “Molecular cloning and sequence of partial cDNA for interferon-induced (2′-5′)oligo(A) synthetase mRNA from human cells”. Proc. Natl. Acad. Sci. U.S.A. 80 (16): 4904\u20138. Bibcode:1983PNAS…80.4904M. doi:10.1073\/pnas.80.16.4904. PMC\u00a0384155. PMID\u00a06348777.Maruyama K, Sugano S (1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1\u20132): 171\u20134. doi:10.1016\/0378-1119(94)90802-8. PMID\u00a08125298.Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K,  et\u00a0al. (1997). “Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library”. Gene. 200 (1\u20132): 149\u201356. doi:10.1016\/S0378-1119(97)00411-3. PMID\u00a09373149.Ghosh A, Sarkar SN, Guo W,  et\u00a0al. (1998). “Enzymatic activity of 2′-5′-oligoadenylate synthetase is impaired by specific mutations that affect oligomerization of the protein”. J. Biol. Chem. 272 (52): 33220\u20136. doi:10.1074\/jbc.272.52.33220. PMID\u00a09407111.Hovnanian A, Rebouillat D, Mattei MG,  et\u00a0al. (1998). “The human 2′,5′-oligoadenylate synthetase locus is composed of three distinct genes clustered on chromosome 12q24.2 encoding the 100-, 69-, and 40-kDa forms”. Genomics. 52 (3): 267\u201377. doi:10.1006\/geno.1998.5443. PMID\u00a09790745.Sarkar SN, Ghosh A, Wang HW,  et\u00a0al. (1999). “The nature of the catalytic domain of 2′-5′-oligoadenylate synthetases”. J. Biol. Chem. 274 (36): 25535\u201342. doi:10.1074\/jbc.274.36.25535. PMID\u00a010464285.       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/oas1-wikipedia\/#breadcrumbitem","name":"OAS1 – Wikipedia"}}]}]